Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Ribonuclease U(1) splits only the phosphodiester bonds of guanosine 3'-phosphates in RNA. It may be regarded as a guanyloribonuclease [ribonucleate (guanine nucleotide)-2'-transferase (cyclizing), EC 2.7.7.26] similar to ribonuclease T(1) (Egami, Takahashi & Uchida, 1964). It seems to be identical with the extracellular ribonuclease described by Glitz & Dekker (1963, 1964a,b). 2. Ribonucleases U(2) and U(3) are novel enzymes with a strict specificity. They split the internucleotide bonds between purine 3'-nucleotides and 5'-hydroxy groups of adjacent nucleotides in RNA with the intermediary formation of purine nucleoside 2',3'-(cyclic)-phosphates, which are slowly hydrolysed to purine 3'-nucleotides. So they may be classified as ;puryloribonucleases [ribonucleate (purine nucleotide)-2'-transferase (cyclizing)]'. Double-stranded RNA is scarcely split by ribonucleases U(2) and U(3). 3. Ribonuclease U(4) has no absolute base specificity, and produces the mononucleotides 3'-adenylate, 3'-guanylate, 3'-cytidylate and 3'-uridylate from RNA.
...
PMID:Studies on extracellular ribonucleases of Ustilago sphaerogena. Characterization of substrate specificity with special reference to purine-specific ribonucleases. 563 16

The nucleolar lesions provoked by the action of ribonuclease (RNase) on living chick embryo fibroblasts were studied by means of microcinematographic analysis and at the ultrastructural level using oxidized diaminobenzidine as a differentially contrasting stain for nucleic acids. This study has shown that the induction of nucleolar dispersion by RNase was only the beginning of a series of discrete steps. The following sequences are described: dispersion of the nucleolus into fragments, their reassembly, and the emission of spherules which appear of chromatin origin. At that step nucleoli are typically segregated. The alteration of the nucleolar associated chromatin seemed to be primordial in these processes. Moreover, the large mass of heterochromatin intimately associated with the nucleolus and which has been considered to be a part of the nucleolar organizer region apparently plays a chief part in the reassembly of the nucleolar fragments into a segregated nucleolus. Ribonuclease is compared to other drugs known to act on nucleolar DNA.
...
PMID:[Nucleolar lesions induced by ribonuclease in living cultured cells]. 619 60

Ribonuclease hydration in wide concentration and temperature range using differential scanning microcalorimetry and NMR technique was studied. The temperature- concentration equilibrium diagram for H2O--ribonuclease system was suggested. Protein hydration in D2O was shown to be higher than in ordinary water. NMR measurements in dilute protein solutions showed that cooperative temperature denaturation was followed by solvation changes. Models of globular protein hydration are discussed.
...
PMID:[Ribonuclease hydration and its heat stability in solutions of H2O and D2O]. 624 23

The broadening of spin-label absorption lines resulting from spin-exchange reactions that occur during collision with paramagnetic Ni2+ is diminished when Ni2+ binds to phospholipid vesicles. Subsequent addition of non-paramagnetic ions that compete for binding sites releases Ni2+ into solution and restores the line-broadening. The concentrations of various ions required to achieve this effect was used to order the ions with respect to their binding to vesicles containing phosphatidylethanolamine and phosphatidylglycerol. The relative strengths of binding for those ions studied were: Ca2+ > Mg2+ > Zn2+ > Sr2+ > Ba2+. The spin-broadening assay was also used to study the effects of two proteins on the availability of Ni2+-binding sites on the vesicles. Ribonuclease, which is thought to associate electrostatically as an extrinsic protein on the surface of vesicles, completely blocked the Ni2+-binding sites at comparatively low protein concentrations. Quantitative considerations of these data suggest the possibility that Ni2+ may bind preferenetially to phosphatidylglycerol, and that these binding sites are aggregated in the ribonuclease-containing vesicles. In contract to ribonuclease, cytochrome c does not block Ni2+-bindings sites on the phospholipid vesicles, but rather contains sites of its own that bind Ni2+, both when the protein is in solution and when it is associated with the vesicles. These results are consistent with other studies which suggest that cytochrome c becomes partially embedded in membrane bilayers and associates with phospholipid molecules through hydrophobic interactions.
...
PMID:Interaction of divalent cations and proteins with phospholipid vesicles. 625 May 97

The isolation and characterization of the initial intermediates formed during the irreversible acid denaturation of enzyme Ribonuclease A are described. The products obtained when RNase A is maintained in 0.5 M HCl at 30 degrees for periods up to 20 h have been analyzed by ion-exchange chromatography on Amberlite XE-64. Four distinct components were found to elute earlier to RNase A; these have been designated RNase Aa2, Aa1c, Aa1b, and Aa1a in order of their elution. With the exception of RNase Aa2, the other components are nearly as active as RNase A. Polyacrylamide gel electrophoresis at near-neutral pH indicated that RNase Aa1a, Aa1b, and Aa1c are monodeamidated derivatives of RNase A; RNase Aa1c contains, in addition, a small amount of a dideamidated component. RNase Aa2, which has 75% enzymic activity as compared to RNase A, consists of dideamidated and higher deamidated derivatives of RNase A. Except for differences in the proteolytic susceptibilities at an elevated temperature or acidic pH, the monodeamidated derivatives were found to have very nearly the same enzymic activity and the compact folded structure as the native enzyme. Fingerprint analyses of the tryptic peptides of monodeamidated derivatives have shown that the deamidations are restricted to an amide cluster in the region 67-74 of the polypeptide chain. The initial acid-catalyzed deamidation occurs in and around the 65-72 disulfide loop giving rise to at least three distinct monodeamidated derivatives of RNase A without an appreciable change in the catalytic activity and conformation of the ribonuclease molecule. Significance of this specific deamidation occurring in highly acidic conditions, and the biological implications of the physiological deamidation reactions of proteins are discussed.
...
PMID:Isolation and characterization of monodeamidated derivatives of bovine pancreatic ribonuclease A. 642 73

The primary structure of ribonuclease F1, the guanine specific ribonuclease from Fusarium moniliforme, has been determined. Ribonuclease F1 consists of 106 amino acid residues and has a molecular weight of 10,980. It has a pyroglutamyl residue at the N-terminus. Comparison of the primary structures of four fungal ribonucleases so far sequenced shows that the amino acid sequences around the assumed active site residues are indeed well conserved. However, structurally important half cystine residues are arranged variously.
...
PMID:The primary structure of ribonuclease F1 from Fusarium moniliforme. 643 32

The present study was carried out to establish the best method of preparing human testicular tissue for flow cytometric DNA analysis including dispersal, fixation and staining. Human testicular tissue could be dispersed to single cells by incubating in 0.05% collagenase solution at 37 degrees C for 60 minutes. Krishan's method which stains nuclear DNA directly without ethanol fixation and digestion in ribonuclease was not suitable for testicular cells. After ethanol fixation, testicular cells were treated with ribonuclease and pepsin, then stained with propidium iodide. Nuclear DNA in cells was measured by flow cytometry and a good DNA histogram was obtained. Ribonuclease influenced the DNA histogram little, but pepsin markedly improved it by digesting cell debris and decreasing cell aggregation. Analysis of the DNA histogram revealed the proportion of haploid, diploid and tetraploid cells accurately and quickly. Flow cytometric DNA analysis could be a useful method of evaluating cell kinetics in spermatogenesis.
...
PMID:[DNA flow cytometric evaluation of spermatogenesis. Part 1: Analysis of nuclear DNA in cells from the human testicular tissue]. 651 92

Ribonuclease inhibitors were purified from the latent ribonuclease fractions of porcine thyroid and liver and used to test the hypothesis that their inhibition of bovine pancreatic ribonuclease A is correctly described by tight-binding rather than Michaelis-Menton kinetics. Both proteins were found to act as slow, tight-binding inhibitors of the enzyme. These steady-state velocities also showed that both the thyroid and liver inhibitors were competitive inhibitors of bovine pancreatic ribonuclease A with Ki's of 0.1 and 0.4 nM, respectively. In contrast to interpretations based on Michaelis-Menton assumptions that show non-competitive inhibition, these results suggest that an enzyme:inhibitor:substrate complex does not exist.
...
PMID:The ribonuclease inhibitors from porcine thyroid and liver are slow, tight-binding inhibitors of bovine pancreatic ribonuclease A. 661 10

A method for electrophoretic concentration of differently charged proteins is described. A nonlinear pH gradient is generated by imposing a potential gradient on an electrolyte system composed of (+)H3PO4-valine (pI 6.0)-Servalyte (pH 9-11)-triethylamine(-). Proteins contained in the valine solution accumulate at the interphase formed between the valine solution and the Servalyte solution. This interphase acts as a barrier or liquid membrane to all proteins having isoelectric points in the range 6-9. For proteins having isoelectric points in the range 5-7 valine is replaced by histidine (pI 7.64) and the Servalyte by Pharmalyte, pH 2.5-5.0. Ribonuclease, hexokinase, bovine serum albumin, and hemoglobin were concentrated and recovered from the top of the column using a peristaltic pump. The duration of concentration process was 1-4 h, the length of the run depending on the experiment scale (20 or 100 ml protein solution), the amount of protein, and the isoelectric point of the protein. Proteins were concentrated 9- to 48-fold, depending on the initial volume and concentration of the protein. The recoveries ranged from 79.7 +/- 1.1 for hemoglobin to 93.17 +/- 2.84 for ribonuclease.
...
PMID:Electrophoretic concentration of proteins in a nonlinear pH gradient. 673 3

Ribonuclease F1, the guanine-specific ribonuclease of Fusarium moniliforme, was purified to homogeneity by a combination of ethanol fractionation, affinity chromatography and DEAE-cellulose column chromatography. The adsorbent for the affinity chromatography was synthesized by the coupling of periodate-oxidized guanosine 5'-monophosphate to aminohexyl agarose followed by sodium borohydride reduction. Ribonuclease F2, the minor component, was also purified to near homogeneity by the same procedure. Ribonucleases F1 and F2 had the same molecular weight (about 11,000) as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. They also showed the same amino acid composition and differed only in the isoelectric point: 4.10 for F1 and 3.96 for F2.
...
PMID:Purification by affinity chromatography and physicochemical properties of the guanine-specific ribonuclease of Fusarium moniliforme. 678 May 47


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---